人血小板前列腺素内过氧化物合酶（环氧化酶）的免疫亲和纯化及cDNA克隆

Immunoaffinity purification and cDNA cloning of human platelet prostaglandin endoperoxide synthase (cyclooxygenase).

作者信息

Takahashi Y, Ueda N, Yoshimoto T, Yamamoto S, Yokoyama C, Miyata A, Tanabe T, Fuse I, Hattori A, Shibata A

机构信息

Department of Biochemistry, Tokushima University School of Medicine, Japan.

出版信息

Biochem Biophys Res Commun. 1992 Jan 31;182(2):433-8. doi: 10.1016/0006-291x(92)91750-k.

DOI:10.1016/0006-291x(92)91750-k

PMID:1734857

Abstract

The cDNA for prostaglandin endoperoxide synthase (cyclooxygenase) was cloned from human platelets by the polymerase chain reaction amplification method, and the primary structure of the enzyme was deduced from the nucleotide sequence. The enzyme was composed of 599 amino acids including 23-amino acid signal sequence, and the calculated molecular weight of the mature protein was 65,995. The enzyme was immunoaffinity-purified from human platelets. The N-terminal amino acid sequence determined by Edman degradation was Ala-Asp-Pro-Gly-Ala-Pro-Thr-Pro-, and the result confirmed the primary structure of the enzyme, which was deduced from the cDNA sequence.

摘要

通过聚合酶链反应扩增法从人血小板中克隆出前列腺素内过氧化物合酶（环氧化酶）的互补脱氧核糖核酸（cDNA），并根据核苷酸序列推导该酶的一级结构。该酶由599个氨基酸组成，包括一个23个氨基酸的信号序列，成熟蛋白的计算分子量为65,995。该酶是从人血小板中通过免疫亲和纯化得到的。通过埃德曼降解法测定的N端氨基酸序列为Ala-Asp-Pro-Gly-Ala-Pro-Thr-Pro-，该结果证实了从cDNA序列推导得出的酶的一级结构。